715
Original Paper
Cell Physiol Biochem 2011;28:715-724 Accepted: September 19, 2011
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CFTR and TMEM16A are Separate but Functionally
Related Cl
-
Channels
Jiraporn Ousingsawat
#
, Patthara Kongsuphol
#
, Rainer Schreiber and
Karl Kunzelmann
Institut für Physiologie, Universität Regensburg, Regensburg,
#
JO and PK share first authorship
Karl Kunzelmann
Institut für Physiologie, Universität Regensburg
Universitätsstraße 31, 93053 Regensburg (Germany)
Tel. +49 (0)941 943 4302, Fax +49 (0)941 943 4315
E-Mail karl.kunzelmann@vkl.uni-regensburg.de
Key Words
Ca
2+
activated Cl
-
currents CaCC TMEM16A CFTR
Cystic fibrosis CF
Abstract
Previous reports point out to a functional relationship
of the cystic fibrosis transmembrane conductance
regulator (CFTR) and Ca
2+
activated Cl
-
channels
(CaCC). Recent findings showing that TMEM16A
forms the essential part of CaCC, prompted us to
examine whether CFTR controls TMEM16A. Inhibition
of endogenous CaCC by activation of endogenous
CFTR was found in 16HBE human airway epithelial
cells, which also express TMEM16A. In contrast,
CFBE airway epithelial cells lack of CFTR expression,
but express TMEM16A along with other TMEM16-
proteins. These cells produce CaCC that is inhibited
by overexpression and activation of CFTR. In HEK293
cells coexpressing TMEM16A and CFTR, whole cell
currents activated by IMBX and forskolin were
significantly reduced when compared with cells
expressing CFTR only, while the halide permeability
sequence of CFTR was not changed. Expression of
TMEM16A, but not of TMEM16F, H or J, produced
robust CaCC, which that were inhibited by CaCCinh-
A01 and niflumic acid, but not by CFTRinh-172.
TMEM16A-currents were attenuated by additional
expression of CFTR, and were completely abrogated
when additionally expressed CFTR was activated by
IBMX and forskolin. On the other hand, CFTR-
currents were attenuated by additional expression of
TMEM16A. CFTR and TMEM16A were both
membrane localized and could be coimmuno-
precipitated. Intracellular Ca
2+
signals elicited by
receptor-stimulation was not changed during
activation of CFTR, while ionophore-induced rise in
[Ca
2+
]
i
was attenuated after stimulation of CFTR. The
data indicate that both CFTR and TMEM16 proteins
are separate molecular entities that show functional
and molecular interaction.
Introduction
The cystic fibrosis transmembrane conductance
regulator (CFTR) is regarded as a cAMP/PKA/ATP-
regulated Cl
-
channel that also controls the function of
other membrane proteins [1]. Apart from the well
examined effects of CFTR on epithelial Na
+
conductance,
it has also been reported earlier that CFTR inhibits